5EZ3
Crystal structure Acyl-CoA dehydrogenase from Brucella melitensis in complex with FAD
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
C | 0000166 | molecular_function | nucleotide binding |
C | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
D | 0000166 | molecular_function | nucleotide binding |
D | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 31 |
Details | binding site for residue FAD A 600 |
Chain | Residue |
A | MET190 |
A | TRP433 |
A | GLU434 |
A | SER436 |
A | ASN438 |
A | LEU442 |
A | HOH740 |
A | HOH747 |
A | HOH751 |
A | HOH777 |
A | HOH807 |
A | MET192 |
A | HOH848 |
A | HOH927 |
B | ARG332 |
B | VAL334 |
B | PHE335 |
B | LEU339 |
B | GLN342 |
B | MET345 |
B | GLU407 |
B | CYS408 |
A | THR193 |
B | GLY410 |
B | GLY411 |
A | GLY197 |
A | GLY198 |
A | THR199 |
A | PHE224 |
A | SER226 |
A | VAL429 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue MRD A 601 |
Chain | Residue |
A | LEU141 |
A | CYS142 |
A | THR145 |
A | ASP309 |
A | ALA313 |
A | ASN430 |
A | TRP433 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue MPD A 602 |
Chain | Residue |
A | ASP301 |
A | PHE370 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue CAC A 603 |
Chain | Residue |
A | LEU548 |
A | HOH769 |
A | HOH996 |
site_id | AC5 |
Number of Residues | 29 |
Details | binding site for residue FAD B 600 |
Chain | Residue |
A | ARG332 |
A | VAL334 |
A | PHE335 |
A | LEU339 |
A | GLN342 |
A | MET345 |
A | GLU407 |
A | CYS408 |
A | GLY410 |
A | GLY411 |
B | MET190 |
B | MET192 |
B | THR193 |
B | GLY197 |
B | GLY198 |
B | THR199 |
B | PHE224 |
B | SER226 |
B | VAL429 |
B | TRP433 |
B | GLU434 |
B | SER436 |
B | ASN438 |
B | LEU442 |
B | HOH720 |
B | HOH724 |
B | HOH777 |
B | HOH782 |
B | HOH841 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue MRD B 601 |
Chain | Residue |
B | LEU141 |
B | CYS142 |
B | THR145 |
B | ASP309 |
B | ALA313 |
B | ASN430 |
B | TRP433 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue CAC B 603 |
Chain | Residue |
B | PRO33 |
B | GLY511 |
B | ALA512 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue CAC B 604 |
Chain | Residue |
B | GLN163 |
B | TRP164 |
B | ALA180 |
B | PHE181 |
site_id | AC9 |
Number of Residues | 29 |
Details | binding site for residue FAD C 600 |
Chain | Residue |
C | LEU442 |
C | HOH765 |
C | HOH776 |
C | HOH795 |
C | HOH797 |
C | HOH812 |
C | HOH825 |
D | ARG332 |
D | VAL334 |
D | LEU339 |
D | GLN342 |
D | MET345 |
D | GLU407 |
D | CYS408 |
D | GLY410 |
D | GLY411 |
C | MET190 |
C | MET192 |
C | THR193 |
C | GLY197 |
C | GLY198 |
C | THR199 |
C | PHE224 |
C | SER226 |
C | VAL429 |
C | TRP433 |
C | GLU434 |
C | SER436 |
C | ASN438 |
site_id | AD1 |
Number of Residues | 8 |
Details | binding site for residue MRD C 601 |
Chain | Residue |
C | LEU141 |
C | CYS142 |
C | THR145 |
C | ASP309 |
C | CYS310 |
C | ALA313 |
C | ASN430 |
C | TRP433 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue CAC C 603 |
Chain | Residue |
C | PRO33 |
C | LEU34 |
C | GLY511 |
C | ALA512 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue CAC C 604 |
Chain | Residue |
C | GLN163 |
C | TRP164 |
C | ALA180 |
C | PHE181 |
site_id | AD4 |
Number of Residues | 30 |
Details | binding site for residue FAD D 600 |
Chain | Residue |
C | ARG332 |
C | VAL334 |
C | PHE335 |
C | LEU339 |
C | GLN342 |
C | MET345 |
C | GLU407 |
C | CYS408 |
C | GLY410 |
C | GLY411 |
D | MET190 |
D | MET192 |
D | THR193 |
D | GLY197 |
D | GLY198 |
D | THR199 |
D | PHE224 |
D | SER226 |
D | VAL429 |
D | TRP433 |
D | GLU434 |
D | SER436 |
D | ASN438 |
D | VAL439 |
D | LEU442 |
D | HOH724 |
D | HOH730 |
D | HOH776 |
D | HOH777 |
D | HOH843 |
site_id | AD5 |
Number of Residues | 7 |
Details | binding site for residue MRD D 601 |
Chain | Residue |
D | PHE130 |
D | LEU141 |
D | CYS142 |
D | THR145 |
D | ASP309 |
D | ASN430 |
D | TRP433 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue CAC D 604 |
Chain | Residue |
D | GLN163 |
D | TRP164 |
D | PHE181 |
D | HOH785 |
Functional Information from PROSITE/UniProt